Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Dihydrolipoyl dehydrogenase, mitochondrial (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (Glycine cleavage system L protein)

 DLDH_DICDI              Reviewed;         488 AA.
Q54EW8; Q6S4V6;
08-APR-2008, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 1.
22-NOV-2017, entry version 92.
RecName: Full=Dihydrolipoyl dehydrogenase, mitochondrial;
EC=1.8.1.4;
AltName: Full=Dihydrolipoamide dehydrogenase;
AltName: Full=Glycine cleavage system L protein;
Flags: Precursor;
Name=lpd; Synonyms=bkdD, dld, odhC, pdhD; ORFNames=DDB_G0291648;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-357.
PubMed=15003488; DOI=10.1016/j.ijpara.2003.11.025;
Huang J., Mullapudi N., Sicheritz-Ponten T., Kissinger J.C.;
"A first glimpse into the pattern and scale of gene transfer in
Apicomplexa.";
Int. J. Parasitol. 34:265-274(2004).
-!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
protein N(6)-(lipoyl)lysine + NADH.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
Note=Binds 1 FAD per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}.
-!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AAFI02000177; EAL61808.1; -; Genomic_DNA.
EMBL; AY466389; AAS47709.1; -; Genomic_DNA.
RefSeq; XP_635122.1; XM_630030.1.
ProteinModelPortal; Q54EW8; -.
SMR; Q54EW8; -.
STRING; 44689.DDB0216232; -.
PaxDb; Q54EW8; -.
PRIDE; Q54EW8; -.
EnsemblProtists; EAL61808; EAL61808; DDB_G0291648.
GeneID; 8628069; -.
KEGG; ddi:DDB_G0291648; -.
dictyBase; DDB_G0291648; lpd.
eggNOG; KOG1335; Eukaryota.
eggNOG; COG1249; LUCA.
InParanoid; Q54EW8; -.
KO; K00382; -.
OMA; TMSEAVM; -.
PhylomeDB; Q54EW8; -.
Reactome; R-DDI-389661; Glyoxylate metabolism and glycine degradation.
Reactome; R-DDI-6783984; Glycine degradation.
Reactome; R-DDI-70268; Pyruvate metabolism.
Reactome; R-DDI-70895; Branched-chain amino acid catabolism.
Reactome; R-DDI-71064; Lysine catabolism.
Reactome; R-DDI-71403; Citric acid cycle (TCA cycle).
PRO; PR:Q54EW8; -.
Proteomes; UP000002195; Chromosome 6.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0005759; C:mitochondrial matrix; ISS:dictyBase.
GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; ISS:dictyBase.
GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; ISS:dictyBase.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0006546; P:glycine catabolic process; ISS:dictyBase.
GO; GO:0006550; P:isoleucine catabolic process; ISS:dictyBase.
GO; GO:0006564; P:L-serine biosynthetic process; ISS:dictyBase.
GO; GO:0006552; P:leucine catabolic process; ISS:dictyBase.
GO; GO:0006574; P:valine catabolic process; ISS:dictyBase.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
InterPro; IPR006258; Lipoamide_DH.
InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
InterPro; IPR012999; Pyr_OxRdtase_I_AS.
Pfam; PF07992; Pyr_redox_2; 1.
Pfam; PF02852; Pyr_redox_dim; 1.
PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
SUPFAM; SSF51905; SSF51905; 1.
SUPFAM; SSF55424; SSF55424; 1.
TIGRFAMs; TIGR01350; lipoamide_DH; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
3: Inferred from homology;
Complete proteome; Disulfide bond; FAD; Flavoprotein; Mitochondrion;
NAD; Oxidoreductase; Redox-active center; Reference proteome;
Transit peptide.
TRANSIT 1 25 Mitochondrion. {ECO:0000255}.
CHAIN 26 488 Dihydrolipoyl dehydrogenase,
mitochondrial.
/FTId=PRO_0000327450.
NP_BIND 52 61 FAD. {ECO:0000250}.
NP_BIND 163 165 FAD. {ECO:0000250}.
NP_BIND 200 207 NAD. {ECO:0000250}.
NP_BIND 341 344 FAD. {ECO:0000250}.
ACT_SITE 467 467 Proton acceptor. {ECO:0000250}.
BINDING 70 70 FAD. {ECO:0000250}.
BINDING 134 134 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 223 223 NAD. {ECO:0000250}.
BINDING 257 257 NAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 294 294 NAD; via amide nitrogen. {ECO:0000250}.
BINDING 335 335 FAD. {ECO:0000250}.
DISULFID 61 66 Redox-active. {ECO:0000250}.
SEQUENCE 488 AA; 51794 MW; A7DD67E8F7707783 CRC64;
MLRINRISNL RTFGQRFFST EQQDVVVIGG GPGGYVAGIK AGQLGMKVTV VEKRGKLGGT
CLNVGCIPSK ALLNASHLYE EATTKMSKYG VKCSGVELDL GAMMQYKDKS VSGLTSGIEG
LFKKNKVKYD KGFGKITGPN TVEVTLNDGS VKTIETKNIV IATGSEVTSL PNVNIDEESI
ISSTGALALK SVPKKLIVIG GGVIGLELGS VWSRLGSETT VVEFTNRIAA GADGEVAKKF
QKSLEKQHMK FHLETKVTSV VKKSDGKVTV TVEQVGAGGF TGTLEADAVL VSVGRRPNTS
GLGLESVGIP TDKAGRVEVG DHFNTKVPSI FAIGDAIRGP MLAHKAEEEG IAIIEQIHNG
GGHVNYGAIP SIIYTHPEVA WVGKTEEELQ KEGIQYNIGR FPFVANSRAK TNDDVEGFVK
FLAAKDSDRV LGAHIMGTNA GELIGECVLA MEYGASCEDI ARTCHGHPTL SEAVKEAAMD
AYDKPIHM


Related products :

Catalog number Product name Quantity
EIAAB11372 Dihydrolipoamide dehydrogenase,Dihydrolipoyl dehydrogenase, mitochondrial,DLD,GCSL,Glycine cleavage system L protein,Homo sapiens,Human,LAD,PHE3
27-169 DLD is the L protein of the mitochondrial glycine cleavage system. The L protein, also named dihydrolipoamide dehydrogenase, is also a component of the pyruvate dehydrogenase complex, the alpha-ketogl 0.05 mg
18-783-77883 RABBIT ANTI PORCINE LIPOAMIDE DEHYDROGENASE - EC 1.8.1.4; Dihydrolipoamide dehydrogenase; Pyruvate dehydrogenase complex E3 subunit; PDC-E3; E3; Glycine cleavage system L protein Polyclonal 1 ml
EIAAB11371 Dihydrolipoamide dehydrogenase,Dihydrolipoyl dehydrogenase, mitochondrial,Dld,Mouse,Mus musculus
EIAAB11375 Dihydrolipoamide dehydrogenase,Dihydrolipoyl dehydrogenase, mitochondrial,Dld,Rat,Rattus norvegicus
EIAAB11374 Dihydrolipoamide dehydrogenase,Dihydrolipoyl dehydrogenase, mitochondrial,DLD,LAD,Pig,Sus scrofa
EIAAB11373 Canis familiaris,Canis lupus familiaris,Dihydrolipoamide dehydrogenase,Dihydrolipoyl dehydrogenase, mitochondrial,DLD,Dog
26-849 The enzyme system for cleavage of glycine (glycine cleavage system; EC 2.1.2.10), which is confined to the mitochondria, is composed of 4 protein components P protein (a pyridoxal phosphate-dependent 0.05 mg
GCSH_RAT Rat ELISA Kit FOR Glycine cleavage system H protein, mitochondrial 96T
CSB-EL009335RA Rat Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit 96T
E0627h Mouse ELISA Kit FOR Glycine cleavage system H protein, mitochondrial 96T
GCSH_CHICK Chicken ELISA Kit FOR Glycine cleavage system H protein, mitochondrial 96T
TT30A_HUMAN Mouse ELISA Kit FOR Glycine cleavage system H protein, mitochondrial 96T
CSB-EL009335RA Rat Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit SpeciesRat 96T
CSB-EL009335HU Human Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit 96T
CSB-EL009335BO Bovine Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit 96T
CSB-EL009335CH Chicken Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit 96T
CSB-EL009335MO Mouse Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit 96T
CSB-EL009335HU Human Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit SpeciesHuman 96T
CSB-EL009335MO Mouse Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit SpeciesMouse 96T
CSB-EL009335BO Bovine Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit SpeciesBovine 96T
CSB-EL009335CH Chicken Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit SpeciesChicken 96T
CSB-EL009335RB Rabbit Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit SpeciesRabbit 96T
GCSH_MOUSE ELISA Kit FOR Glycine cleavage system H protein, mitochondrial; organism: Mouse; gene name: Gcsh 96T
EIAAB28692 Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex,Lipoyl-containing pyruvate dehydrogenase complex component X,Mouse,Mus musculus,Pdhx,Pyruvate dehydrogenase protein X c


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur